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Small Alarmone Synthetases as novel bacterial RNA-binding proteins
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS). University of Tartu, Institute of Technology, Tartu, Estonia.
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
2017 (English)In: RNA Biology, ISSN 1547-6286, E-ISSN 1555-8584, Vol. 14, no 12, p. 1695-1699Article, review/survey (Refereed) Published
Abstract [en]

The alarmone nucleotides guanosine pentaphosphate (pppGpp) and tetraphosphate (ppGpp), collectively referred to as (p)ppGpp, are key regulators of bacterial growth, stress adaptation, antibiotic tolerance and pathogenicity. We have recently shown that the Small Alarmone Synthetase (SAS) RelQ from the Gram-positive pathogen Enterococcus faecalis has an RNA-binding activity (Beljantseva et al. 2017). RelQ's activities as an enzyme and as an RNA-binding protein are mutually incompatible: binding of single-stranded RNA potently inhibits (p)ppGpp synthesis in a sequence-specific manner, and RelQ's enzymatic activity destabilizes the RNA: RelQ complex. RelQ's allosteric regulator, pppGpp, destabilizes RNA binding and activates RelQ's enzymatic activity. Since SAS enzymes are widely distributed in bacteria, and, as has been discovered recently, are also mobilized by phages (Dedrick et al. 2017), RNA binding to SASs could be a widespread mechanism. The initial discovery raises numerous questions regarding RNA-binding function of the SAS enzymes: What is the molecular mechanism underlying the incompatibility of RNA: SAS complex formation with pppGpp binding and (p)ppGpp synthesis? What are the RNA targets in living cells? What is the regulatory output of the system - (p)ppGpp synthesis, modulation of RNA structure and function, or both?

Place, publisher, year, edition, pages
Taylor & Francis, 2017. Vol. 14, no 12, p. 1695-1699
Keyword [en]
ppGpp, RelQ, SAS, RSH, stringent response, RNA, nucleotide, RNA-binding protein, Hfq, CsrA
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-144879DOI: 10.1080/15476286.2017.1367889ISI: 000423291400011PubMedID: 28820325OAI: oai:DiVA.org:umu-144879DiVA, id: diva2:1184453
Available from: 2018-02-21 Created: 2018-02-21 Last updated: 2018-06-09Bibliographically approved

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Hauryliuk, VasiliAtkinson, Gemma C.

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